WO2003070276A1 - A preparation and method for weight reduction - Google Patents

A preparation and method for weight reduction Download PDF

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Publication number
WO2003070276A1
WO2003070276A1 PCT/FI2003/000107 FI0300107W WO03070276A1 WO 2003070276 A1 WO2003070276 A1 WO 2003070276A1 FI 0300107 W FI0300107 W FI 0300107W WO 03070276 A1 WO03070276 A1 WO 03070276A1
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WO
WIPO (PCT)
Prior art keywords
amino acids
trypsin
essential amino
trypsin inhibitor
preparation
Prior art date
Application number
PCT/FI2003/000107
Other languages
French (fr)
Inventor
Pia Heino
Original Assignee
Remedal Oy
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Remedal Oy filed Critical Remedal Oy
Priority to EP03702672A priority Critical patent/EP1482976B1/en
Priority to US10/504,148 priority patent/US20050096266A1/en
Priority to DE60323062T priority patent/DE60323062D1/en
Priority to AU2003205795A priority patent/AU2003205795A1/en
Priority to CA002476771A priority patent/CA2476771A1/en
Priority to JP2003569231A priority patent/JP2005523284A/en
Publication of WO2003070276A1 publication Critical patent/WO2003070276A1/en

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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
    • A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/55—Protease inhibitors
    • A61K38/56—Protease inhibitors from plants
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P3/00—Drugs for disorders of the metabolism
    • A61P3/04—Anorexiants; Antiobesity agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00

Definitions

  • This invention relates to weight reduction by taking with meals a formula in accordance with the invention.
  • Chained carbohydrates are degraded to monosaccharides, proteins are degraded to peptides and amino acids, and fats are degraded to free fatty acids and cholesterol.
  • nutrients are used by the body as structural components of tissues, cells, enzymes, antibodies, etc.
  • proteins are composed of 20 L-amino acids. Eleven of these amino acids can be synthesised by the human body (nonessential amino acids), whereas nine amino acids are such that the body cannot produce (essential amino acids). The latter must therefore be obtained from the diet.
  • the adult daily protein requirement is about 60 g, with essential amino acids accounting for about 9 g of this amount.
  • appetite suppressants e.g. amfepramone, fenfluramine and sibutramine
  • side effects such as insomnia, blood pressure elevation and, in the case of the two first-mentioned drugs, also drug dependence.
  • Fenfluramine furthermore, has caused heart valve disease, leading to its withdrawal from the market in most countries.
  • Orlistat too, has specific side effects which limit its usefulness.
  • the present invention provides a remedy to the unsatisfactory state of affairs described above.
  • the hepaticopancreatic duct which empties into the duodenum somewhat distally from the pylorus, starts to discharge trypsinogen, an inactive proenzyme secreted by the pancreas.
  • the wall of the duodenum contains an enzyme called enterokinase. Enterokinase converts the inactive trypsinogen to active trypsin which in turn breaks down the chyme-contained proteins into peptides. Trypsin further activates other enzymes responsible for the digestion of food proteins. Trypsin also activates any remaining trypsinogen through an autocatalytic mechanism.
  • the 50 - 100 mg of trypsin secreted in conjunction with eating is able to break down into peptides all of the 30-60 g of protein contained in a normal meal. Without the action of trypsin, this digestion of protein will not take place.
  • pancreatic diseases sometimes progressing to complete cessation of trypsin secretion.
  • enzyme preparation e.g. Pancreatin®. Twin Laboratories Inc., Hauppauge, NY, USA
  • digests food proteins thus makes up for the lacking trypsin secretion.
  • trypsin inhibitors most of which are proteins by nature. In the presence of trypsin, these compounds bind to trypsin, forming inactive complexes.
  • Well known trypsin inhibitors include alpha 1 -antitrypsin, trypstatin, alpha 2-macroglobulin, soybean trypsin inhibitors, egg-white trypsin inhibitors and aprotinin. Each of these is available commercially, and the latter substance is also registered as a medicinal product (e.g. Trasylol®. Bayer AG, Leverkusen, Germany).
  • Therapeutic oral administration of trypsin inhibitors and trypsin inactivation in the alimentary tract have been published for instance in patent documents JP 2-250823 (A) and US 5607671.
  • the present invention is aimed at preventing the absorption of proteins. This is achieved by oral administration of one, of the above-mentioned trypsin inhibitors with meals whereby the trypsin inhibitor moves along the alimentary tract to trypsin's site of action in the intestine.
  • soybean trypsin inhibitor Type ll-S. Sigma Chemical Co., St. Louis, MO, USA
  • one weight unit of the inhibitor can inactivate 2.5 weight units of trypsin secreted into the duodenum by the pancreas.
  • the proteins contained in the food are not digested and cannot be absorbed. This results in artificial protein malabsorption which inevitably leads to loss of body weight.
  • the present invention includes oral coadministration of required amounts of all essential amino acids in free form, together with the trypsin inhibitor.
  • the essential amino acids are L- phenylalanine, L-histidine, L-isoleucine, L-leucine, L-lysine, L-methionine, L- threonine, L-tryptophan and L-valine. While weight is lost, these essential amino acids prevent the development of malabsorption syndrome.
  • the nonessential amino acids do not function as required by the invention, they cannot by used as active substances in its embodiments. Free amino acids are fully absorbed from the alimentary tract, and their absorption is not affected by the trypsin inhibitor.
  • the present invention allows the amount of absorbed food protein and the energy therein to be reduced without causing a deficiency of essential amino acids.
  • the result is weight reduction without disturbance of the nutritional status of the body.
  • the trypsin inhibitor is preferably transported to trypsin's site of action in the intestine in a formulation that does not release the active substance until it has passed the stomach. This is achieved by application of a "programmed delivery pattern" in the pharmaceutical formulation.
  • enteric coating suitable for embodiments of the invention include polyvinyl acetate (Colorcon®. Colorcon Inc., West Point, PA, USA) and the acrylic acid derivatives described in patent document JP 2-250823 (A).
  • Said enteric coatings dissolve when the ambient pH exceeds 4.7. As such pH is characteristic of the intestine right from the beginning of the duodenum, release of the active substance is accomplished exactly in this desired location below the stomach. It then mixes with trypsin in the chyme, causing inhibition of trypsin activity.
  • the person concerned is not required to subdue, limit or regulate his/her hunger or appetite in any way.
  • One dose of a preparation in accordance with the invention is as follows:
  • Said dose (2 g) may be formulated, for instance, as a sachet or capsule containing a single-dose of powder or as a tablet containing the powder in combination with approved excipients or, for instance, an aqueous solution of approved excipients and the active ingredients.
  • any nontoxic compound that inactivates trypsin can be used for trypsin inhibition.
  • Proteinous trypsin inhibitors can be enteric encapsulated, for instance, by coating microgranules with polyvinyl acetate (Colorcon®). Such granules can be administered either on their own or, for instance, in a gelatine capsule together with essential amino acids, or the two entities can be taken as separate preparations, albeit during the same meal.

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • General Health & Medical Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Animal Behavior & Ethology (AREA)
  • Medicinal Chemistry (AREA)
  • Epidemiology (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Botany (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • General Chemical & Material Sciences (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Organic Chemistry (AREA)
  • Immunology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Hematology (AREA)
  • Child & Adolescent Psychology (AREA)
  • Diabetes (AREA)
  • Obesity (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Medicines Containing Plant Substances (AREA)
  • Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
  • Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
  • Coloring Foods And Improving Nutritive Qualities (AREA)
  • Medicinal Preparation (AREA)
  • Saccharide Compounds (AREA)
  • Diaphragms For Electromechanical Transducers (AREA)

Abstract

The present invention encompasses a preparation and method whereby a trypsin inhibitor and free essential amino acids are used simultaneously in the form of an oral preparation to reduce weight.

Description

A preparation and method for weight reduction
This invention relates to weight reduction by taking with meals a formula in accordance with the invention.
A person weighing 70 kg consumes on average 10 MJ of energy per 24 hours. Of this energy, 45% is derived from carbohydrate, 20% from protein and 35% from fat. These figures correspond to approximately 260 g carbohydrate, 120 g protein and 90 g fat. It is also apparent that the energy content per unit weight of latter group of nutrients is more than twice that of the other two groups. After a meal, these energy-yielding nutrients are degraded by digestive enzymes to a form optimal for absorption from the gastrointestinal tract into the blood stream. On average, 85% of the carbohydrate, 95% of the fat and 80% of the protein is absorbed. Chained carbohydrates are degraded to monosaccharides, proteins are degraded to peptides and amino acids, and fats are degraded to free fatty acids and cholesterol. Apart from being a source of energy, nutrients are used by the body as structural components of tissues, cells, enzymes, antibodies, etc. Such use is almost exclusively limited to proteins. Proteins are composed of 20 L-amino acids. Eleven of these amino acids can be synthesised by the human body (nonessential amino acids), whereas nine amino acids are such that the body cannot produce (essential amino acids). The latter must therefore be obtained from the diet. The adult daily protein requirement is about 60 g, with essential amino acids accounting for about 9 g of this amount. In cases of insufficient protein intake from food, the liver is able to synthesise enough of all nonessential amino acids from carbohydrates and fats. If, however, there is a lack of essential amino acids in food, the affected person will develop malabsorption syndrome manifested as kwashiorkor. This disease is mainly encountered in developing countries.
If the amount of energy contained in absorbed food exceeds the energy consumption of the body, the excess will be stored in the body in the form of fat. In the industrialized world, where the population has access to a rich diet, this often leads to overweight with associated adverse effects on health. It has proved difficult therapeutically to eliminate overweight or to reduce it to any significant extent. The available treatment options comprise eating less, following a low-calorie diet, energy consuming exercise and pharmacological therapy. Each of these alternatives requires that the patient is highly motivated to lose weight and receives continuous mental support in this effort. Even so, normal weight is often not attained, and any reasonably good result tends to be obliterated by a gradual return to original weight after the end of the treatment.
The currently known appetite suppressants, e.g. amfepramone, fenfluramine and sibutramine, are associated with side effects such as insomnia, blood pressure elevation and, in the case of the two first-mentioned drugs, also drug dependence. Fenfluramine, furthermore, has caused heart valve disease, leading to its withdrawal from the market in most countries. Treatment of obesity with orlistat, an inhibitor of fat absorption, calls for good motivation to lose weight and a low-fat diet. Orlistat, too, has specific side effects which limit its usefulness.
The present invention provides a remedy to the unsatisfactory state of affairs described above.
After a meal, the hepaticopancreatic duct, which empties into the duodenum somewhat distally from the pylorus, starts to discharge trypsinogen, an inactive proenzyme secreted by the pancreas. The wall of the duodenum contains an enzyme called enterokinase. Enterokinase converts the inactive trypsinogen to active trypsin which in turn breaks down the chyme-contained proteins into peptides. Trypsin further activates other enzymes responsible for the digestion of food proteins. Trypsin also activates any remaining trypsinogen through an autocatalytic mechanism. The 50 - 100 mg of trypsin secreted in conjunction with eating is able to break down into peptides all of the 30-60 g of protein contained in a normal meal. Without the action of trypsin, this digestion of protein will not take place.
The above situation occurs in certain pancreatic diseases, sometimes progressing to complete cessation of trypsin secretion. These patients have to take with meals an enzyme preparation (e.g. Pancreatin®. Twin Laboratories Inc., Hauppauge, NY, USA) that digests food proteins and thus makes up for the lacking trypsin secretion.
The action of trypsin can be prevented by trypsin inhibitors, most of which are proteins by nature. In the presence of trypsin, these compounds bind to trypsin, forming inactive complexes. Well known trypsin inhibitors include alpha 1 -antitrypsin, trypstatin, alpha 2-macroglobulin, soybean trypsin inhibitors, egg-white trypsin inhibitors and aprotinin. Each of these is available commercially, and the latter substance is also registered as a medicinal product (e.g. Trasylol®. Bayer AG, Leverkusen, Germany). Therapeutic oral administration of trypsin inhibitors and trypsin inactivation in the alimentary tract have been published for instance in patent documents JP 2-250823 (A) and US 5607671.
The present invention is aimed at preventing the absorption of proteins. This is achieved by oral administration of one, of the above-mentioned trypsin inhibitors with meals whereby the trypsin inhibitor moves along the alimentary tract to trypsin's site of action in the intestine. When for instance soybean trypsin inhibitor (Type ll-S. Sigma Chemical Co., St. Louis, MO, USA) is used in accordance with the invention, one weight unit of the inhibitor can inactivate 2.5 weight units of trypsin secreted into the duodenum by the pancreas. As the action of trypsin is thus inhibited, the proteins contained in the food are not digested and cannot be absorbed. This results in artificial protein malabsorption which inevitably leads to loss of body weight.
Nevertheless, such usage of trypsin inhibitor alone causes not only weight loss but in the long run even malabsorption syndrome. The present invention, therefore, includes oral coadministration of required amounts of all essential amino acids in free form, together with the trypsin inhibitor. The essential amino acids are L- phenylalanine, L-histidine, L-isoleucine, L-leucine, L-lysine, L-methionine, L- threonine, L-tryptophan and L-valine. While weight is lost, these essential amino acids prevent the development of malabsorption syndrome. Of all amino acids, only the above-mentioned ones constitute a part of the invention. Since the nonessential amino acids do not function as required by the invention, they cannot by used as active substances in its embodiments. Free amino acids are fully absorbed from the alimentary tract, and their absorption is not affected by the trypsin inhibitor.
The present invention allows the amount of absorbed food protein and the energy therein to be reduced without causing a deficiency of essential amino acids. The result is weight reduction without disturbance of the nutritional status of the body.
For of the above-described effect to be achieved, the invention is characterized by the features presented in the patent claims.
As protein structure can be altered by the action of hydrochloric acid and pepsin in the stomach, the trypsin inhibitor is preferably transported to trypsin's site of action in the intestine in a formulation that does not release the active substance until it has passed the stomach. This is achieved by application of a "programmed delivery pattern" in the pharmaceutical formulation.
An applicable technique for this purpose is for instance microgranulation in combination with enteric coating which protects the active substance against the digestive effect of gastric juice. Enteric coatings suitable for embodiments of the invention include polyvinyl acetate (Colorcon®. Colorcon Inc., West Point, PA, USA) and the acrylic acid derivatives described in patent document JP 2-250823 (A).
Said enteric coatings dissolve when the ambient pH exceeds 4.7. As such pH is characteristic of the intestine right from the beginning of the duodenum, release of the active substance is accomplished exactly in this desired location below the stomach. It then mixes with trypsin in the chyme, causing inhibition of trypsin activity.
The present invention affords the following novel and unexpected advantages over prior art:
- The person trying to lose weight does not have to change his/her habitual diet in any way even if this particular diet were the cause of the person's overweight. - No changes are required in the daily amount of food ingested by the person, i.e. his/her daily intake of energy from food, even if the amount of energy contained in those very same meals were the cause of the person's overweight.
And still the person will lose weight.
The inventiveness of the present invention is further enhanced by the fact that
- it involves no effort to control the feeling of hunger or appetite of the person who is trying to lose weight
and the fact that
- the person concerned is not required to subdue, limit or regulate his/her hunger or appetite in any way.
Exemplifying embodiment
One dose of a preparation in accordance with the invention is as follows:
Soybean trypsin inhibitor 150 mg
L-Phenylalanine 250 mg
L-Histidine 200 mg
L-lsoleucine 200 mg
L-Leucine 250 mg
L-Lysine 200 mg
L-Methionine 200 mg
L-Threonine 200 mg
L-Tryptophan 150 mg
L-Valine 200 mg
Said dose (2 g) may be formulated, for instance, as a sachet or capsule containing a single-dose of powder or as a tablet containing the powder in combination with approved excipients or, for instance, an aqueous solution of approved excipients and the active ingredients.
Totally five doses (10 g) of the formula presented above are taken with daily meals in one of the pharmaceutical formulations presented above. This amount is sufficient and adequate to satisfy the daily requirement for all essential amino acids.
In accordance with the invention, any nontoxic compound that inactivates trypsin can be used for trypsin inhibition. Proteinous trypsin inhibitors can be enteric encapsulated, for instance, by coating microgranules with polyvinyl acetate (Colorcon®). Such granules can be administered either on their own or, for instance, in a gelatine capsule together with essential amino acids, or the two entities can be taken as separate preparations, albeit during the same meal.

Claims

Patent claims
1. An oral preparation for reducing weight, characterized in that the formula of the preparation contains simultaneously all the essential amino acids in free form and in addition a trypsin inhibitor as active substances.
2. Use of a trypsin inhibitor and essential amino acids for producing an oral preparation according to claim 1 , for reducing weight.
3. Use of a trypsin inhibitor and essential amino acids in a therapeutic method for reducing weight, in which a) a trypsin inhibitor is administered in the form of an oral preparation to prevent the absorption of food-contained proteins from the alimentary tract and b) free essential amino acids are administered in the form of an oral preparation to make up for the essential amino acids contained in said unabsorbed proteins.
PCT/FI2003/000107 2002-02-20 2003-02-12 A preparation and method for weight reduction WO2003070276A1 (en)

Priority Applications (6)

Application Number Priority Date Filing Date Title
EP03702672A EP1482976B1 (en) 2002-02-20 2003-02-12 A preparation and method for weight reduction
US10/504,148 US20050096266A1 (en) 2002-02-20 2003-02-12 Preparation and method for weight reduction
DE60323062T DE60323062D1 (en) 2002-02-20 2003-02-12 PREPARATION AND METHOD FOR WEIGHT REDUCTION
AU2003205795A AU2003205795A1 (en) 2002-02-20 2003-02-12 A preparation and method for weight reduction
CA002476771A CA2476771A1 (en) 2002-02-20 2003-02-12 A preparation and method for weight reduction
JP2003569231A JP2005523284A (en) 2002-02-20 2003-02-12 Formulation and method for weight loss

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
FI20020332 2002-02-20
FI20020332A FI20020332A0 (en) 2002-02-20 2002-02-20 Preparation and method of weight loss

Publications (1)

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WO2003070276A1 true WO2003070276A1 (en) 2003-08-28

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PCT/FI2003/000107 WO2003070276A1 (en) 2002-02-20 2003-02-12 A preparation and method for weight reduction

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US (1) US20050096266A1 (en)
EP (1) EP1482976B1 (en)
JP (1) JP2005523284A (en)
CN (1) CN1729017A (en)
AT (1) ATE405290T1 (en)
AU (1) AU2003205795A1 (en)
CA (1) CA2476771A1 (en)
DE (1) DE60323062D1 (en)
ES (1) ES2314175T3 (en)
FI (1) FI20020332A0 (en)
WO (1) WO2003070276A1 (en)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP2067411A1 (en) * 2007-11-29 2009-06-10 Paolo Oddenino Paris S.R.L. Food composition usable as substitute meal
EP2148580A1 (en) * 2007-04-26 2010-02-03 HealthSpan Solutions, LLC Compositions and approaches for increasing diet induced thermogenesis, inducing weight loss and maintaining muscles mass and strength

Citations (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB652237A (en) * 1945-12-27 1951-04-18 Merck & Co Inc Therapeutic amino acid mixtures
US4042687A (en) * 1975-11-24 1977-08-16 Control Drug, Inc. Method of treating obesity by the oral administration of a predigested protein composition
US4491578A (en) * 1982-06-14 1985-01-01 Peikin Steven R Method of stimulating satiety in mammals
EP0301122A1 (en) * 1986-01-31 1989-02-01 Hiroshi Maeda Use of soybean kunitz type trypsin and derivatives in the preparation of medicaments and agent comprising the same
JPH02250823A (en) * 1989-03-24 1990-10-08 Tsumura & Co Microcapsule agent and production thereof
ES2087027A1 (en) * 1994-08-03 1996-07-01 Univ Illes Balears Thermogenic nutritional supplements, foods that contain them, and applications.
US5607671A (en) * 1992-01-17 1997-03-04 Heino; Pekka U. Medical use, a medical method and a pharmaceutical preparation
WO2002002103A2 (en) * 2000-07-04 2002-01-10 Professional Dietetics S.R.L. Compositions based on aminoacids, suitable for the treatment of heart failure
JP2002154976A (en) * 2000-11-22 2002-05-28 Sanpo Kk Agent and health food for preventing, ameliorating and/ or treating chronic disease

Patent Citations (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB652237A (en) * 1945-12-27 1951-04-18 Merck & Co Inc Therapeutic amino acid mixtures
US4042687A (en) * 1975-11-24 1977-08-16 Control Drug, Inc. Method of treating obesity by the oral administration of a predigested protein composition
US4491578A (en) * 1982-06-14 1985-01-01 Peikin Steven R Method of stimulating satiety in mammals
EP0301122A1 (en) * 1986-01-31 1989-02-01 Hiroshi Maeda Use of soybean kunitz type trypsin and derivatives in the preparation of medicaments and agent comprising the same
JPH02250823A (en) * 1989-03-24 1990-10-08 Tsumura & Co Microcapsule agent and production thereof
US5607671A (en) * 1992-01-17 1997-03-04 Heino; Pekka U. Medical use, a medical method and a pharmaceutical preparation
ES2087027A1 (en) * 1994-08-03 1996-07-01 Univ Illes Balears Thermogenic nutritional supplements, foods that contain them, and applications.
WO2002002103A2 (en) * 2000-07-04 2002-01-10 Professional Dietetics S.R.L. Compositions based on aminoacids, suitable for the treatment of heart failure
JP2002154976A (en) * 2000-11-22 2002-05-28 Sanpo Kk Agent and health food for preventing, ameliorating and/ or treating chronic disease

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
DATABASE WPI Week 199633, Derwent World Patents Index; Class B04, AN 1996-323071, XP002966482 *
DATABASE WPI Week 200259, Derwent World Patents Index; Class B04, AN 2002-552774, XP002966481 *
PATENT ABSTRACTS OF JAPAN vol. 14, no. 571 (C - 790) 19 December 1990 (1990-12-19) *

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP2148580A1 (en) * 2007-04-26 2010-02-03 HealthSpan Solutions, LLC Compositions and approaches for increasing diet induced thermogenesis, inducing weight loss and maintaining muscles mass and strength
EP2148580A4 (en) * 2007-04-26 2010-10-13 Healthspan Solutions Llc Compositions and approaches for increasing diet induced thermogenesis, inducing weight loss and maintaining muscles mass and strength
EP2067411A1 (en) * 2007-11-29 2009-06-10 Paolo Oddenino Paris S.R.L. Food composition usable as substitute meal

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Publication number Publication date
JP2005523284A (en) 2005-08-04
AU2003205795A1 (en) 2003-09-09
EP1482976B1 (en) 2008-08-20
FI20020332A0 (en) 2002-02-20
CA2476771A1 (en) 2003-08-28
ES2314175T3 (en) 2009-03-16
EP1482976A1 (en) 2004-12-08
DE60323062D1 (en) 2008-10-02
CN1729017A (en) 2006-02-01
ATE405290T1 (en) 2008-09-15
US20050096266A1 (en) 2005-05-05

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